This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Research in the California State University and several predominantly undergraduate institutions involves the determination of the 3-D structures of proteins, peptides and enzymes of importance in bionanotechnology, biomedicine, environmental and industrial processes. This request for beam time at SSRL focuses on the collection of high resolution diffraction data from bacterial cytochromes c?, a novel myosin folding chaperone from Drosophila melanogaster, yeast carbonyl reductase mutants, single cysteine flavoprotein NAD(P)H oxidoreductases involved in sulfur reduction, a novel RNA safeguard enzyme TM0159 from Thermatoga maritima, recombinant beta-secretase in complex with natural product inhibitors, several dehydrogenases (complexes and mutants), and bio-zeolites based on helical peptides. The desire to collect data at SSRL is based upon our need for high quality, high resolution diffraction data from a number of different crystals, some of which are either too small or sensitive for conventional x-ray sources. While the majority of protein structures can be determined by molecular replacement, at least one requires accurate MAD data collection.